1EF2

CRYSTAL STRUCTURE OF MANGANESE-SUBSTITUTED KLEBSIELLA AEROGENES UREASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0009039	molecular_function	urease activity
A	0016151	molecular_function	nickel cation binding
A	0016787	molecular_function	hydrolase activity
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A	0043419	biological_process	urea catabolic process
A	0046872	molecular_function	metal ion binding
B	0005737	cellular_component	cytoplasm
B	0009039	molecular_function	urease activity
B	0016787	molecular_function	hydrolase activity
B	0035550	cellular_component	urease complex
B	0043419	biological_process	urea catabolic process
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0009039	molecular_function	urease activity
C	0016151	molecular_function	nickel cation binding
C	0016787	molecular_function	hydrolase activity
C	0019627	biological_process	urea metabolic process
C	0043419	biological_process	urea catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MN A 4774

Chain	Residue
A	HOH500
A	HOH501
A	KCX1217
A	HIS1219
A	HIS1246
A	HIS1272
A	GLY1277
A	MN4775

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN A 4775

Chain	Residue
A	HOH502
A	HIS1134
A	HIS1136
A	KCX1217
A	ASP1360
A	MN4774
A	HOH500

---

Functional Information from PROSITE/UniProt

site_id	PS00145
Number of Residues	17
Details	UREASE_2 Urease active site. MVCHHLdpdIaeDVaFA

Chain	Residue	Details
A	MET1317-ALA1333

---

site_id	PS01120
Number of Residues	14
Details	UREASE_1 Urease nickel ligands signature. TAGGIDtHIHwicP

Chain	Residue	Details
A	THR1127-PRO1140

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"description":"via carbamate group"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01953","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10913264","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7754395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8702515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8718850","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1kra

Chain	Residue	Details
A	HIS1219
A	ARG1336
A	HIS1320
A	ASP1221

---

site_id	MCSA1
Number of Residues	10
Details	M-CSA 87

Chain	Residue	Details
A	HIS1134	metal ligand
A	MET1364	activator, metal ligand
A	HIS1136	metal ligand
A	KCX1217	activator, metal ligand
A	GLY1223	proton acceptor, proton donor, proton relay
A	THR1225	activator, proton acceptor, proton donor
A	LEU1250	metal ligand
A	ALA1276	metal ligand
A	PRO1324	proton acceptor, proton donor
A	GLU1340	activator

---